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Unfolding the Mysteries of Protein Metamorphosis. ACS Chem Biol 2018 06 15;13(6):1438-1446

Date

05/23/2018

Pubmed ID

29787234

Pubmed Central ID

PMC6007232

DOI

10.1021/acschembio.8b00276

Scopus ID

2-s2.0-85047568358   8 Citations

Abstract

Since the proposal of Anfinsen's thermodynamic hypothesis in 1963, our understanding of protein folding and dynamics has gained significant appreciation of its nuance and complexity. Intrinsically disordered proteins, chameleonic sequences, morpheeins, and metamorphic proteins have broadened the protein folding paradigm. Here, we discuss noncanonical protein folding patterns, with an emphasis on metamorphic proteins, and we review known metamorphic proteins that occur naturally and that have been engineered in the laboratory. Finally, we discuss research areas surrounding metamorphic proteins that are primed for future exploration, including evolution, drug discovery, and the quest for previously unrecognized metamorphs. As we enter an age where we are capable of complex bioinformatic searches and de novo protein design, we are primed to search for previously unrecognized metamorphic proteins and to design our own metamorphs to act as targeted, switchable drugs; biosensors; and more.

Author List

Dishman AF, Volkman BF

Author

Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Bacteria
Humans
Intrinsically Disordered Proteins
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Engineering
Protein Folding
Protein Unfolding
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46